Serine 123 phosphorylation modulates p21 protein stability and activity by suppressing ubiquitin-independent proteasomal degradation

Journal of Biological Chemistry

Volumn 287, Issue 41, 2012, Pages 34410-34418

  Chen, Xiangling ^a   Zhang, Jin ^a   Zhang, Min ^a   Liu, Shou ^a   Yan, Wensheng ^a   Jung, JinHyuk ^a   Chen, Xinbin ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE; CELLULAR PROCESS; CYCLIN-DEPENDENT KINASE INHIBITORS; HIGH MOLECULAR MASS; ISOFORMS; LOW MOLECULAR MASS; ORTHOLOGS; PROTEASOMAL DEGRADATION; PROTEIN STABILITY; STRESS RESPONSE; TUMORIGENESIS;

CELL DEATH; CELL PROLIFERATION; CLONING; GENE ENCODING; MEDICAL PROBLEMS; PHOSPHORYLATION; PROTEINS;

AMINO ACIDS;

ISOPROTEIN; MUTANT PROTEIN; PROLINE; PROTEASOME; PROTEIN P21; SERINE; UBIQUITIN;

ANIMAL CELL; ARTICLE; CELL PROLIFERATION; CONTROLLED STUDY; DOG; ENZYME REPRESSION; HALF LIFE TIME; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; REGULATORY MECHANISM;

ANIMALS; CELL LINE; CELL PROLIFERATION; CYCLIN-DEPENDENT KINASE INHIBITOR P21; DOGS; HUMANS; PHOSPHORYLATION; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN ISOFORMS; PROTEIN STABILITY; PROTEOLYSIS; SERINE; SPECIES SPECIFICITY; UBIQUITIN;

EID: 84867240307     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.384990     Document Type: Article

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